AT18B_ARATH
ID AT18B_ARATH Reviewed; 366 AA.
AC Q8H1Q8; Q9M0A9;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Autophagy-related protein 18b;
DE Short=AtATG18b;
GN Name=ATG18B; OrderedLocusNames=At4g30510; ORFNames=F17I23.150;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-366.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND TISSUE SPECIFICITY.
RX PubMed=15860012; DOI=10.1111/j.1365-313x.2005.02397.x;
RA Xiong Y., Contento A.L., Bassham D.C.;
RT "AtATG18a is required for the formation of autophagosomes during nutrient
RT stress and senescence in Arabidopsis thaliana.";
RL Plant J. 42:535-546(2005).
CC -!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis
CC and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC Required for autophagy (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex at least
CC composed of ATG18, SAC/FIG4, FAB1 and VAC14. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Peripheral membrane protein of pre-autophagosomal structure (PAS)
CC and vacuole. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8H1Q8-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers and leaves.
CC {ECO:0000269|PubMed:15860012}.
CC -!- DOMAIN: The first protein part may form a beta-propeller domain
CC involved in specific binding to phosphatidylinositol 3,5-bisphosphate
CC (PIP2), leading to the association of the protein to the membrane.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB79769.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL161577; CAB79769.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85774.2; -; Genomic_DNA.
DR EMBL; AY142529; AAN13072.1; -; mRNA.
DR PIR; H85356; H85356.
DR RefSeq; NP_001320091.1; NM_001342010.1. [Q8H1Q8-1]
DR RefSeq; NP_001320092.1; NM_001342011.1.
DR AlphaFoldDB; Q8H1Q8; -.
DR SMR; Q8H1Q8; -.
DR BioGRID; 14461; 1.
DR STRING; 3702.AT4G30510.1; -.
DR iPTMnet; Q8H1Q8; -.
DR PaxDb; Q8H1Q8; -.
DR PRIDE; Q8H1Q8; -.
DR ProteomicsDB; 246819; -. [Q8H1Q8-1]
DR EnsemblPlants; AT4G30510.1; AT4G30510.1; AT4G30510. [Q8H1Q8-1]
DR GeneID; 829174; -.
DR Gramene; AT4G30510.1; AT4G30510.1; AT4G30510. [Q8H1Q8-1]
DR KEGG; ath:AT4G30510; -.
DR Araport; AT4G30510; -.
DR TAIR; locus:2118801; AT4G30510.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_3_0_1; -.
DR InParanoid; Q8H1Q8; -.
DR OMA; NNKGLCA; -.
DR OrthoDB; 1216824at2759; -.
DR PRO; PR:Q8H1Q8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8H1Q8; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Autophagy; Membrane; Protein transport;
KW Reference proteome; Repeat; Transport; Vacuole; WD repeat.
FT CHAIN 1..366
FT /note="Autophagy-related protein 18b"
FT /id="PRO_0000421880"
FT REPEAT 6..44
FT /note="WD 1"
FT REPEAT 178..218
FT /note="WD 2"
FT REPEAT 223..265
FT /note="WD 3"
SQ SEQUENCE 366 AA; 39877 MW; 46714BF2726A91CC CRC64;
MANLSSLPSP IYCVSFNQDN SGFAISWKDS FKIFDSTTGR LCYERAAGAF VIVEMLYSSD
LLAIVGAGEQ ASLSPRRLCL FKTTTGLPLR ELNFLTSILA VRMNKKRLVV VLLEKTFVYD
LNTLVMLDTI DTVPNPKGLS AFSPSLEGCY LAVPASTTKG SVLVYNVMDL QSHSEIDAHR
SPLAAIALSS NGMYIATGSE QGTLIRVHLV SEATKSYSFR RGTYPSTIYS LSFGPSTQLP
DILIATSSSG SIHAFSLSLA INQRSKRSTS FLGSVLPDSV SDALDPAHHH VLQNAVSSGI
RSYAVVRKID KLEGTSSPSH FTSLRATVSV ITYNGYFQEY TLSINNKNES LWTLEREFNL
FSITTG
